Japanese clinical practice guidelines for aspiration and pharyngeal residual assessment during eating and swallowing for nursing care.

AIM: This clinical practice guideline aims to provide and recommend methods of assessing aspiration and pharyngeal residue during eating and swallowing and methods of selecting and implementing nursing care for adults to prevent the development of aspiration pneumonia through early and appropriate management of oropharyngeal dysphagia. METHODS: In April 2018, the Japan Academy of Nursing Science established the Supervisory Committee in Nursing Care Development/Standardization Committee to develop clinical practice guidelines for aspiration and pharyngeal residual assessment during eating and swallowing for nursing care. This clinical practice guideline was developed according to the Minds Manual for Guideline Development 2017, with the aim of providing a specific pathway for nurses to determine the policy for selecting management for oropharyngeal dysphagia based on research evidence and multifaceted factors including the balance of benefits and harms and patients' values. RESULTS: Based on the 10 clinical questions related to assessment by physical assessment, the Repetitive Saliva Swallowing Test, Modified Water Swallowing Test, Food Test, cervical auscultation, observation using an ultrasound diagnostic device, and an endoscope, 10 recommendations have been developed. Eight recommendations have been evaluated as the Grading of Recommendations Assessment, Development and Evaluation (GRADE) 2C, and the other two have been evaluated as no GRADE. CONCLUSION: The first reliable clinical practice guideline has been produced from an academic nursing organization that focuses on assessment for nursing care and incorporates the latest findings.

Protection of cardiomyocytes from the hypoxia-mediated injury by a peptide targeting the activator of G-protein signaling 8.

Signaling via heterotrimeric G-protein is involved in the development of human diseases including ischemia-reperfusion injury of the heart. We previously identified an ischemia-inducible G-protein activator, activator of G-protein signaling 8 (AGS8), which regulates Gßγ signaling and plays a key role in the hypoxia-induced apoptosis of cardiomyocytes. Here, we attempted to intervene in the AGS8-Gßγ signaling process and protect cardiomyocytes from hypoxia-induced apoptosis with a peptide that disrupted the AGS8-Gßγ interaction. Synthesized AGS8-peptides, with amino acid sequences based on those of the Gßγ-binding domain of AGS8, successfully inhibited the association of AGS8 with Gßγ. The AGS8-peptide effectively blocked hypoxia-induced apoptosis of cardiomyocytes, as determined by DNA end-labeling and an increase in cleaved caspase-3. AGS8-peptide also inhibited the change in localization/permeability of channel protein connexin 43, which was mediated by AGS8-Gßγ under hypoxia. Small compounds that inhibit a wide range of Gßγ signals caused deleterious effects in cardiomyocytes. In contrast, AGS8-peptide did not cause cell damage under normoxia, suggesting an advantage inherent in targeted disruption of the AGS8-Gßγ signaling pathway. These data indicate a pivotal role for the interaction of AGS8 with Gßγ in hypoxia-induced apoptosis of cardiomyocytes, and suggest that targeted disruption of the AGS8-Gßγ signal provides a novel approach for protecting the myocardium against ischemic injury.

Purification, cDNA cloning, and expression profiles of the cyclobutane pyrimidine dimer photolyase of Xenopus laevis.

Photolyase is a light-dependent enzyme that repairs pyrimidine dimers in DNA. Two types of photolyases have been found in frog Xenopus laevis, one for repairing cyclobutane pyrimidine dimers (CPD photolyase) and the other for pyrimidine-pyrimidone (6-4)photoproduct [(6-4)photolyase]. However, little is known about the former type of the Xenopus photolyases. To characterize this enzyme and its expression profiles, we isolated the entire coding region of a putative CPD photolyase cDNA by extending an EST (expressed sequence tag) sequence obtained from the Xenopus database. Nucleotide sequence analysis of the cDNA revealed a protein of 557 amino acids with close similarity to CPD photolyase of rat kangaroo. The identity of this cDNA was further established by the molecular mass (65 kDa) and the partial amino acid sequences of the major CPD photolyase that we purified from Xenopus ovaries. The gene of this enzyme is expressed in various tissues of Xenopus. Even internal organs like heart express relatively high levels of mRNA. A much smaller amount was found in skin, although UV damage is thought to occur most frequently in this tissue. Such expression profiles suggest that CPD photolyase may have roles in addition to the photorepair function.